Crystal structure of the anti-CRISPR, AcrIIC4.

Autor: Kim GE; College of Pharmacy, Chung-Ang University, Seoul, Republic of Korea.; Department of Global Innovative Drugs, Graduate School of Chung-Ang University, Seoul, Republic of Korea., Lee SY; College of Pharmacy, Chung-Ang University, Seoul, Republic of Korea.; Department of Global Innovative Drugs, Graduate School of Chung-Ang University, Seoul, Republic of Korea., Park HH; College of Pharmacy, Chung-Ang University, Seoul, Republic of Korea.; Department of Global Innovative Drugs, Graduate School of Chung-Ang University, Seoul, Republic of Korea.
Jazyk: angličtina
Zdroj: Protein science : a publication of the Protein Society [Protein Sci] 2021 Dec; Vol. 30 (12), pp. 2474-2481. Date of Electronic Publication: 2021 Oct 29.
DOI: 10.1002/pro.4214
Abstrakt: Clustered regularly interspaced short palindromic repeats (CRISPRs)-CRISPR-associated protein systems are bacterial and archaeal defense mechanisms against invading elements such as phages and viruses. To overcome these defense systems, phages and viruses have developed inhibitors called anti-CRISPRs (Acrs) that are capable of inhibiting the host CRISPR-Cas system via different mechanisms. Although the inhibitory mechanisms of AcrIIC1, AcrIIC2, and AcrIIC3 have been revealed, the inhibitory mechanisms of AcrIIC4 and AcrIIC5 have not been fully understood and structural data are unavailable. In this study, we elucidated the crystal structure of Type IIC anti-CRISPR protein, AcrIIC4. Our structural analysis revealed that AcrIIC4 exhibited a helical bundle fold comprising four helixes. Further biochemical and biophysical analyses showed that AcrIIC4 formed a monomer in solution, and monomeric AcrIIC4 directly interacted with Cas9 and Cas9/sgRNA complex. Discovery of the structure of AcrIIC4 and their interaction mode on Cas9 will help us elucidate the diversity in the inhibitory mechanisms of the Acr protein family.
(© 2021 The Protein Society.)
Databáze: MEDLINE
Externí odkaz: